4P5P
X-ray structure of Francisella tularensis Rapid Encystment Protein 24 KDa (REP24), gene product of FTN_0841
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-04-05 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.1159 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 44.439, 44.439, 183.454 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 38.486 - 1.540 |
R-factor | 0.1495 |
Rwork | 0.147 |
R-free | 0.19350 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1u9c |
RMSD bond length | 0.007 |
RMSD bond angle | 1.114 |
Data reduction software | DENZO |
Data scaling software | SCALA (3.2.5) |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 61.151 | 91.670 | 1.580 |
High resolution limit [Å] | 1.500 | 4.740 | 1.500 |
Rmerge | 0.095 | 0.056 | 0.226 |
Total number of observations | 237816 | 10242 | 12964 |
Number of reflections | 33819 | ||
<I/σ(I)> | 13.4 | 26.2 | 1.9 |
Completeness [%] | 96.9 | 99.8 | 82.9 |
Redundancy | 7 | 8 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 7.1% (w/v) PEG6000, 0.1M Na-Succinate pH 5.5, 0.58% Heptanoyl-N-methylglucamideMG7 |